Lectin and alliinase are the predominant proteins in nectar from leek (Allium porrum L.) flowers

Peumans, Willy J.; Smeets, Karen; Nerum, Karel Van; Leuven, Fred Van; Damme, Els J.M. Van

doi:10.1007/s004250050070

Cited by 73 publications

(57 citation statements)

References 28 publications

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“…Despite the fact that lectin-expressing GM crops are not commercialized, bees may already be exposed to lectins . Leek (Allium porrum) nectar can contain 0.02% of a mannose-binding lectin, similar to GNA (Peumans et al, 1997). As this concentration lies close to the effect range of about 0.1% as recorded in the above-mentioned studies, a potential insecticidal risk is not excluded.…”

Section: Lectinsmentioning

confidence: 80%

Effects of multiple Bt proteins and GNA lectin on in vitro-reared honey bee larvae

Hendriksma¹,

Härtel²,

Babendreier³

et al. 2012

Apidologie

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-The honey bee is a key non-target arthropod in environmental risk assessments of genetically modified crops. We analyzed for the first time combined effects of three Bt proteins conferring insect resistances, and a CP4-protein conferring an herbicide resistance as simultaneously expressed in one GM maize. Furthermore, the biosafety of Galanthus nivalis agglutinin (GNA lectin), a candidate protein for pest control was tested. Under worst-case exposure scenario, by using controlled in vitro larvae rearing, the combination of Bt proteins showed no adverse effects on bee larvae. In contrast, the GNA lectin was toxic at a 144 h LD 50 of 16.3 μg/larva. The prepupal weight was found to differ between the larvae collection days and between the colonies used for the experiment, explaining up to five times more data variance than the protein treatments (N=709 prepupae). In conclusion, neither single nor a mix of different Bt proteins were found harmful to honey bee larvae.Apis mellifera / Bacillus thuringiensis / environmental risk assessment / genetically modified crops / Cry protein

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Section: Lectinsmentioning

confidence: 80%

Effects of multiple Bt proteins and GNA lectin on in vitro-reared honey bee larvae

Hendriksma¹,

Härtel²,

Babendreier³

et al. 2012

Apidologie

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“…However, these reports have primarily been undetailed investigations, failing to identify the proteins responsible for the respective activities. Only a few investigations have clearly identified the activities of defined nectar proteins (2)(3)(4)(5).…”

Section: Znmentioning

confidence: 99%

Tobacco Nectarin I

Carter

Thornburg

2000

Journal of Biological Chemistry

193

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Nectarin I, a protein that accumulates in the nectar of Nicotiana sp., was determined to contain superoxide dismutase activity by colorimetric and in-gel assays. This activity was found to be remarkably thermostable. did not restore superoxide dismutase activity. The quaternary structure of the reconstituted enzyme was examined, and only tetrameric and pentameric aggregates were enzymatically active. The reconstituted enzyme was also shown to generate H 2 O 2 . Putative nectarin I homologues were found in the nectars of several other plant species.

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“…Lectins, small proteins that are common seed defences, have also been characterised from Erythrina, including E. caffra and E. lys-istemon (Lis et al 1985), and may be present in the nectar. Leek (Allium porrum) nectar contains a mannose-binding lectin (Peumans et al 1997). Nectar of both E. caffra and E. lysistemon has very high amino acid concentrations, including non-protein amino acids (Nicolson 2007), and some amino acids are known to have a bitter taste (Gardener and Gillman 2002).…”

Section: Discussionmentioning

confidence: 99%

Nectar palatability can selectively filter bird and insect visitors to coral tree flowers

et al. 2015

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Secondary compounds in nectar may play a decisive role in determining the spectrum of floral visitors on plants. Flowers of the African coral tree Erythrina caffra are visited mainly by generalist passerine nectarivores, such as weavers and bulbuls. As the nectar of this species tastes very bitter to humans, it was hypothesized that secondary compounds may repel sunbirds and honeybees which are common in the same habitats yet seldom consume the nectar. We conducted choice tests using fresh nectar and both sucrose and hexose (glucose/fructose) solutions of the same concentration as the nectar. White-bellied Sunbirds (Cinnyris talatala) were repelled by nectar of both E. caffra and a related species Erythrina lysistemon, but Dark-capped Bulbuls (Pycnonotus tricolor) did not discriminate between the Erythrina nectar and control sugar solution in terms of amounts consumed. Honeybees (Apis mellifera scutellata) probed exposed droplets of E. caffra nectar and a control sugar solution at the same rate, suggesting that there is no volatile deterrent, but they immediately withdrew their proboscis far more often from the droplets of Erythrina nectar than they did from the sugar solution, suggesting that they find Ery-thrina nectar distasteful. These results contribute to a growing awareness that non-sugar components of nectar can play important functional roles in plant pollination systems.

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Lectin and alliinase are the predominant proteins in nectar from leek (Allium porrum L.) flowers

Cited by 73 publications

References 28 publications

Effects of multiple Bt proteins and GNA lectin on in vitro-reared honey bee larvae

Effects of multiple Bt proteins and GNA lectin on in vitro-reared honey bee larvae

Tobacco Nectarin I

Nectar palatability can selectively filter bird and insect visitors to coral tree flowers

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